ArticleACS chemical biology2012
Identification of high affinity polo-like kinase 1 (Plk1) polo-box domain binding peptides using oxime-based diversification.
Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Affinity enhancement of polo-like kinase 1 polo box domain-binding ligands by a bivalent approach using a covalent kinase-binding component.RSC chemical biology · 2024Article
- A High-Throughput Fluorescence Polarization-Based Assay for the SH2 Domain of STAT4.Methods and protocols · 2022Article
- Development of ultra-high affinity bivalent ligands targeting the polo-like kinase 1.RSC chemical biology · 2022Article
- Design and synthesis of a new orthogonally protected glutamic acid analog and its use in the preparation of high affinity polo-like kinase 1 polo-box domain - binding peptide macrocycles.Organic & biomolecular chemistry · 2021Article
- Phosphonopeptides containing free phosphonic groups: recent advances.RSC advances · 2020Review
- Application of Post Solid-Phase Oxime Ligation to Fine-Tune Peptide-Protein Interactions.Molecules (Basel, Switzerland) · 2020Review
- Peptidomimetic Polo-Box-Targeted Inhibitors that Engage PLK1 in Tumor Cells and Are Selective against the PLK3 Tumor Suppressor.ChemMedChem · 2020Article
- Identification of inhibitors of the polo-box domain of polo-like kinase 1 from natural and semisynthetic compounds.Investigational new drugs · 2020Article
- A cryptic hydrophobic pocket in the polo-box domain of the polo-like kinase PLK1 regulates substrate recognition and mitotic chromosome segregation.Scientific reports · 2019Article
- Development of Highly Selective 1,2,3-Triazole-containing Peptidic Polo-like Kinase 1 Polo-box Domain-binding Inhibitors.Molecules (Basel, Switzerland) · 2019Article
- Targeting Protein-Protein Interactions of Tyrosine Phosphatases with Microarrayed Fragment Libraries Displayed on Phosphopeptide Substrate Scaffolds.ACS combinatorial science · 2019Article
- Histidine N(τ)-cyclized macrocycles as a new genre of polo-like kinase 1 polo-box domain-binding inhibitors.Bioorganic & medicinal chemistry letters · 2018Article
- Enhancing polo-like kinase 1 selectivity of polo-box domain-binding peptides.Bioorganic & medicinal chemistry · 2017Article
- The Emerging Role of Polo-Like Kinase 1 in Epithelial-Mesenchymal Transition and Tumor Metastasis.Cancers · 2017Review
- Several inhibitors of the Plk1 Polo-Box Domain turn out to be non-specific protein alkylators.Cell cycle (Georgetown, Tex.) · 2017Article
- Identification of a novel Polo-like kinase 1 inhibitor that specifically blocks the functions of Polo-Box domain.Oncotarget · 2017Article
- Current progress and future perspectives in the development of anti-polo-like kinase 1 therapeutic agents.F1000Research · 2017Review
- Application of oxime-diversification to optimize ligand interactions within a cryptic pocket of the polo-like kinase 1 polo-box domain.Bioorganic & medicinal chemistry letters · 2016Article
- 4R- and 4S-iodophenyl hydroxyproline, 4R-pentynoyl hydroxyproline, and S-propargyl-4-thiolphenylalanine: conformationally biased and tunable amino acids for bioorthogonal reactions.Organic & biomolecular chemistry · 2016Article
- Recent Advances and New Strategies in Targeting Plk1 for Anticancer Therapy.Trends in pharmacological sciences · 2015Review
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Authors and funding
9 authors.
Funding
Abstract
In an effort to develop improved binding antagonists of the polo-like kinase 1 (Plk1) polo-box domain (PBD), we optimized interactions of the known high affinity 5-mer peptide PLHSpT using oxime-based post solid-phase peptide diversification of the N-terminal Pro residue. This allowed us to achieve up to two orders of magnitude potency enhancement. An X-ray crystal structure of the highest affinity analogue in complex with Plk1 PBD revealed new binding interactions in a hydrophobic channel that had been occluded in X-ray structures of the unliganded protein. This study represents an important example where amino acid modification by post solid-phase oxime ligation can facilitate the development of protein-protein interaction inhibitors by identifying new binding pockets that would not otherwise be accessible to coded amino acid residues.
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